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-Structure paper
Title | Structural Basis for pri-miRNA Recognition by Drosha. |
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Journal, issue, pages | Mol Cell, Vol. 78, Issue 3, Page 423-433.e5, Year 2020 |
Publish date | May 7, 2020 |
Authors | Wenxing Jin / Jia Wang / Chao-Pei Liu / Hong-Wei Wang / Rui-Ming Xu / |
PubMed Abstract | A commencing and critical step in miRNA biogenesis involves processing of pri-miRNAs in the nucleus by Microprocessor. An important, but not completely understood, question is how Drosha, the ...A commencing and critical step in miRNA biogenesis involves processing of pri-miRNAs in the nucleus by Microprocessor. An important, but not completely understood, question is how Drosha, the catalytic subunit of Microprocessor, binds pri-miRNAs and correctly specifies cleavage sites. Here we report the cryoelectron microscopy structures of the Drosha-DGCR8 complex with and without a pri-miRNA. The RNA-bound structure provides direct visualization of the tertiary structure of pri-miRNA and shows that a helix hairpin in the extended PAZ domain and the mobile basic (MB) helix in the RNase IIIa domain of Drosha coordinate to recognize the single-stranded to double-stranded junction of RNA, whereas the dsRNA binding domain makes extensive contacts with the RNA stem. Furthermore, the RNA-free structure reveals an autoinhibitory conformation of the PAZ helix hairpin. These findings provide mechanistic insights into pri-miRNA cleavage site selection and conformational dynamics governing pri-miRNA recognition by the catalytic component of Microprocessor. |
External links | Mol Cell / PubMed:32220645 |
Methods | EM (single particle) |
Resolution | 3.9 - 4.2 Å |
Structure data | EMDB-30005: pri-miRNA bound DROSHA-DGCR8 complex EMDB-30006, PDB-6lxe: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | HYDROLASE/RNA BINDING PROTEIN/RNA / Ribonuclease / RNA BINDING PROTEIN / HYDROLASE-RNA BINDING PROTEIN-RNA complex / HYDROLASE/RNA BINDING PROTEIN / HYDROLASE-RNA BINDING PROTEIN complex |